Zinc transport activity of Fear of Intimacy is essential for proper gonad morphogenesis and DE-cadherin expression

Development. 2006 Mar;133(6):1143-53. doi: 10.1242/dev.02256. Epub 2006 Feb 15.

Abstract

Embryonic gonad formation involves intimate contact between germ cells and specialized somatic cells along with the complex morphogenetic movements necessary to create proper gonad architecture. Previously, we have shown that gonad formation in Drosophila requires the homophilic cell-adhesion molecule Drosophila E-cadherin (DE-cadherin), and also Fear of Intimacy (FOI), which is required for stable accumulation of DE-cadherin protein in the gonad. Here, we present an in vivo structure-function analysis of FOI that strongly indicates that zinc transport activity of FOI is essential for gonad development. Mutant forms of FOI that are defective for zinc transport also fail to rescue morphogenesis and DE-cadherin expression in the gonad. We further show that expression of DE-cadherin in the gonad is regulated post-transcriptionally and that foi affects this post-transcriptional control. Expression of DE-cadherin from a ubiquitous (tubulin) promoter still results in gonad-specific accumulation of DE-cadherin, which is strongly reduced in foi mutants. This work indicates that zinc is a crucial regulator of developmental processes and can affect DE-cadherin expression on multiple levels.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Animals, Genetically Modified
  • Biological Transport
  • Cadherins / genetics
  • Cadherins / metabolism*
  • Conserved Sequence
  • Drosophila Proteins / chemistry
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster / embryology*
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / metabolism*
  • Gene Expression Regulation, Developmental
  • Gonads / embryology*
  • Gonads / metabolism*
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Mutation / genetics
  • Phenotype
  • Protein Processing, Post-Translational
  • RNA, Messenger / genetics
  • Sequence Alignment
  • Zinc / metabolism*

Substances

  • Cadherins
  • Drosophila Proteins
  • Membrane Proteins
  • RNA, Messenger
  • foi protein, Drosophila
  • shg protein, Drosophila
  • Zinc